VirA, a coregulator of Ti-specified virulence genes, is phosphorylated in vitro.
High-level expression of a chimeric virA gene was obtained by replacing the first 524 codons of virA with the first half of trpE. The encoded fusion protein was isolated and found to exhibit autokinase activity. Therefore, a kinase domain is in the C-terminal portion of VirA, and protein phosphorylation may be an important feature of VirA function.
Huang
Y
Y
Department of Plant Pathology, University of California, Davis 95616.
Morel
P
P
Powell
B
B
Kado
C I
CI
D001426:Bacterial Proteins / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D003001:Cloning, Molecular; D005798:Genes, Bacterial; D005809:Genes, Regulator; D010766:Phosphorylation; D011494:Protein Kinases / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000302:isolation & purification / Q000378:metabolism; D015183:Restriction Mapping; D012231:Rhizobium / Q000235:genetics* / Q000378:metabolism / Q000472:pathogenicity; D014774:Virulence / Q000235:genetics; D037521:Virulence Factors
D001426:Bacterial Proteins; D011993:Recombinant Fusion Proteins; D037521:Virulence Factors; D011494:Protein Kinases